Persistent human Borna disease virus infection modifies the acetylome of human oligodendroglia cells towards higher energy and transporter levels

- We used SILAC-based proteomics to analyze the acetylome of BDV infected OL cells.
- We quantified 791Kac sites in 473 proteins.
- Bioinformatic analysis revealed altered acetylation of metabolic proteins et al.
- BDV manipulates the OL acetylome towards higher energy and transporter levels.
- BDV infection is associated with enriched phosphate-associated metabolic processes.

BackgroundBorna disease virus (BDV) is a neurotropic RNA virus persistently infecting mammalian hosts including humans. Lysine acetylation (Kac) is a key protein post-translational modification (PTM). The unexpectedly broad regulatory scope of Kac let us to profile the entire acetylome upon BDV infection.MethodsThe acetylome was profiled through stable isotope labeling for cell culture (SILAC)-based quantitative proteomics. The quantifiable proteome was annotated using bioinformatics.ResultsWe identified and quantified 791 Kac sites in 473 Kac proteins in human BDV Hu-H1-infected and non-infected oligodendroglial (OL) cells. Bioinformatic analysis revealed that BDV infection alters the acetylation of metabolic proteins, membrane-associated proteins and transmembrane transporter activity, and affects the acetylation of several lysine acetyltransferases (KAT).ConclusionsUpon BDV persistence the OL acetylome is manipulated towards higher energy and transporter levels necessary for shuttling BDV proteins to and from nuclear replication sites.

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